Conformational fluctuations in deoxy hemoglobin revealed as a major contributor to anionic modulation of function through studies of the oxygenation and oxidation of hemoglobins A0 and deer lodge β2(NA2)His → Arg

Biochemistry

Volumn 37, Issue 2, 1998, Pages 496-506

  Bonaventura, Celia ^a   Tesh, Shirley ^a   Faulkner, Kevin M ^a   Kraiter, Daniel ^a   Crumbliss, Alvin L ^a  

^a DUKE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN A;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BLOOD OXYGENATION; CONFORMATIONAL TRANSITION; DEER; ENVIRONMENTAL FACTOR; HUMAN; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION;

ANIONS; BINDING SITES; CHLORIDES; HEMOGLOBIN A; HEMOGLOBINS; HEMOGLOBINS, ABNORMAL; OXIDATION-REDUCTION; OXYGEN; PROTEIN CONFORMATION; SULFHYDRYL REAGENTS;

CERVIDAE;

EID: 0032512409     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971574s     Document Type: Article

References (65)

1. Bonaventura, C., and Bonaventura, J. (1978) in Biochemical and Clinical Aspects of Hemoglobin Abnormalities (Caughey, W. S., Ed.) pp 647-663, Academic Press, New York.
2. Bonaventura, C., and Bonaventura, J. (1980) Am. Zool. 20, 131-138.
3. Perutz, M. F. (1989) Q. Rev. Biophys. 22, 139-236.
4. Perutz, M. F., and Imai, K. (1980) J. Mol. Biol. 136, 183-191.
5. Perutz, M. F., Shih, D. T. B., and Williamson, D. (1994) J. Mol. Biol. 239, 555-560.
6. Labossiere, A., Vella, F., Hiebert, J., and Galbraith, P. (1972) Clin. Biochem. 5, 46-50.
7. Busch, M. R., and Ho, C. (1990) Biophys. Chem. 37, 313-322.
8. Bonaventura, J., Bonaventura, C., Sullivan, B., and Godette, G. (1975) J. Biol. Chem. 250, 9250-9255.
9. Bonaventura, C., Arumugam, M., Cashon, R., Bonaventura, J., and Moo-Penn, W. F. (1994) J. Mol. Biol. 239, 561-568.
10. Faulkner, K. M., Bonaventura, C., and Crumbliss, A. L. (1994) Inorg. Chim. Acta 226, 187-194.
11. Faulkner, K. M., Bonaventura, C., and Crumbliss, A. L. (1995) J. Biol. Chem. 270, 13604-13612.
12. Antonini, E., and Brunori, M. (1971) Hemoglobin and Myoglobin in Their Reactions With Ligands, North-Holland Publishing Company, Amsterdam and London.
13. Kilmartin, J. V. (1973) Biochem. J. 133, 725-733.
14. Nagai, K., Luisi, B., Shih, D., Miyazaki, G., Imai, K., Poyart, C., De Young, A., Kwiatkowsky, L., Noble, R. W., Ling, S.-H., and Yu, N.-T. (1987) Nature 329, 858-860.
15. Rivetti, C., Mozzarelli, A., Rossi, G. L., Henry, E. R., and Eaton, W. A. (1993) Biochemistry 32, 2888-2906.
16. Riggs, A. F., and Wolbach, R. A. (1956) J. Gen. Physiol. 39, 585-605.
17. Kristensen, E. E., Igo, D. H., Elder, R. C., and Heineman, W. R. (1991) J. Electroanal. Chem. 309, 61-72.
18. Grassetti, D. R., and Murray, J. F., Jr. (1967) Arch. Biochem. Biophys. 119, 41-49.
19. Focesi, A., Cashon, R. E., Bonaventura, C., and Bonaventura, J. (1983) Fed. Proc. 42, 2030.
20. Cashon, R., Bonaventura, C., and Bonaventura, J. (1986) J. Biol. Chem. 261, 12700-12705.
21. Maeda, T., Hiromi, K., and Shibata, S. (1970) Biochem. Biophys. Res. Commun. 38, 934-939.
22. Taketa, F., and Morell, S. A. (1969) Anal. Biochem. 32, 169-174.
23. Ampulski, R. S., Ayers, V. E., and Morell, S. A. (1969) Anal. Biochem. 32, 163-169.
24. Perutz, M. F. (1978) Sci. Am. 92-123.
25. Perutz, M. F. (1982) Adv. Exp. Med., Biol. 148, 31-48.
26. Lee, A. W., Karplus, M., Poyart, C., and Bursaux, E. (1988) Biochemistry 27, 1285-1301.
27. Ho, C., and Russu, I. M. (1987) Biochemistry 26, 6299-6305.
28. Busch, M. R., Mace, J. E., Ho, N. T., and Ho, C. (1991) Biochemistry 30, 1865-1877.
29. Sun, D. P., Zou, M., Ho, N. T., and Ho, C. (1997) Biochemistry 36, 6663-6673.
30. Perutz, M. F. (1976) Br. Med. Bull. 32, 195-208.
31. Ackers, G. K., Doyle, M. L., Myers, D., and Daughterly, M. A. (1992) Science 255, 54-63.
32. Barrick, D., Ho, N. T., Simplaceanu, V., Dahlquist, F. W., and Ho, C. (1997) Nat. Struct. Biol. 4, 78-83.
33. Perutz, M. F., Fermi, G., Luisi, B., Shaanan, B., and Liddington, R. C. (1987) Accts. Chem. Res. 20, 309-321.
34. Monod, J., Wyman, J., and Changeux, J.-P. (1965) J. Mol. Biol. 12, 88-118.
35. Benesch, R. E., Edalji, R., and Benesch, R. (1977) Biochemistry 16, 2594-2597.
36. Gray, R. D., and Gibson, Q. H. (1971) J. Biol. Chem. 246, 7168-7174.
37. Desbois, A., and Banerjee, R. (1975) J. Mol. Biol. 92, 479-493.
38. Perutz, M. F., Fersht, A. R., Simon, S. R., and Roberts, G. C. K. (1974) Biochemistry 13, 2174-2186.
39. Banerjee, R., and Cassoly, R. (1969) J. Mol. Biol. 42, 337-349.
40. Banerjee, R., and Lhoste, J.-M. (1976) Eur. J. Biochem. 67, 349-356.
41. Ogo, S., Focesi, A., Jr., Cashon, R., Bonaventura, J., and Bonaventura, C. (1989) J. Biol. Chem. 264, 11302-11306.
42. Imai, K. (1973) Biochemistry 12, 128-139.
43. Minton, A. P., and Imai, K. (1974) Proc. Nat. Acad. Sci. 71, 1418-1421.
44. Imai, K. (1982) Allosteric Effects in Haemoglobin, Cambridge University Press, Cambridge.
45. Kister, J., Poyart, C., and Edelstein, S. J. (1987) J. Biol. Chem. 262, 12085-12091.
46. Kister, J., Poyart, C., and Edelstein, S. J. (1987) Biophys. J. 52, 527-535.
47. Marden, M. C., Bohn, B., Kister, J., and Poyart, C. (1990) Biophys. J. 57, 397-403.
48. Perutz, M. F. (1970) Nature 228, 726-734.
49. Arnone, A. (1972) Nature 237, 146-149.
50. Arnone, A., and Perutz, M. F. (1974) Nature 249, 34-36.
51. Benesch, R. E., and Benesch, R. (1970) Fed. Proc. 29, 1101-1104.
52. Nagai, K. (1977) J. Mol. Biol. 111, 41-53.
53. Bonaventura, C., Sullivan, B., Bonaventura, J., and Bourne, S. (1977) Nature 265, 474-476.
54. Perutz, M. F. (1987) in Molecular Basis of Blood Disease (Stammatayanopoulos, G., Nienhuis, A. W., Leder, P., and Majerus, P. W., Eds.) pp 127-178, Saunders, Philadelphia.
55. Szabo, A., and Karplus, M. (1972) J. Mol. Biol. 72, 163-197.
56. Paoli, M., Dodson, G., Liddington, R. C., and Williamson, A. J. (1997) J. Mol. Biol. 271, 161-167.
57. Mansouri, A., and Winterhalter, K. H. (1974) Biochemistry 13, 3311-3314.
58. Edelstein, S. J., and Gibson, Q. H. (1975) J. Biol. Chem. 250, 961-965.
59. Lindstrom, T. R., and Ho, C. (1973) Biochemistry 12, 134-139.
60. Friedman, J. M. (1994) in Methods in Enzymology: Hemoglobins (Everse, J., Vandegriff, K. D., and Winslow, R. M., Eds.) Vol. 232, pp 205-231, Academic Press, San Diego.
61. Miura, S., and Ho, C. (1984) Biochemistry 23, 2492-2499.
62. Mathews, A. J., Olson, J. S., Renaud, J.-P., Tame, J., and Nagai, K. (1991) J. Biol. Chem. 266, 21631-21639.
63. Friend, S. H., Matthew, J. B., and Gurd, F. R. N. (1981) Biochemistry 20, 580-586.
64. Englander, S. W., and Kallenbach, N. R. (1984) Q. Rev. Biophys. 16, 521-655.
65. Rodgers, K. R., Su, C., Subramaniam, S., and Spiro, G. (1992) J. Am. Chem. Soc. 114, 3697-3709.